1z2p
From Proteopedia
(New page: 200px<br /><applet load="1z2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z2p, resolution 1.22Å" /> '''Inositol 1,3,4-trisp...) |
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| - | [[Image:1z2p.gif|left|200px]]<br /><applet load="1z2p" size=" | + | [[Image:1z2p.gif|left|200px]]<br /><applet load="1z2p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z2p, resolution 1.22Å" /> | caption="1z2p, resolution 1.22Å" /> | ||
'''Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3'''<br /> | '''Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Inositol hexakisphosphate and other inositol high polyphosphates have | + | Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with MG, ACP and I3S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Z2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ACP:'>ACP</scene> and <scene name='pdbligand=I3S:'>I3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Eukaryota]] | [[Category: Eukaryota]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hurley, J | + | [[Category: Hurley, J H.]] |
| - | [[Category: Majerus, P | + | [[Category: Majerus, P W.]] |
| - | [[Category: Miller, G | + | [[Category: Miller, G J.]] |
| - | [[Category: Wilson, M | + | [[Category: Wilson, M P.]] |
[[Category: ACP]] | [[Category: ACP]] | ||
[[Category: I3S]] | [[Category: I3S]] | ||
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[[Category: inositol phosphate kinase]] | [[Category: inositol phosphate kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:31 2008'' |
Revision as of 14:11, 21 February 2008
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Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3
Overview
Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.
About this Structure
1Z2P is a Single protein structure of sequence from Eukaryota with , and as ligands. Full crystallographic information is available from OCA.
Reference
Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase., Miller GJ, Wilson MP, Majerus PW, Hurley JH, Mol Cell. 2005 Apr 15;18(2):201-12. PMID:15837423
Page seeded by OCA on Thu Feb 21 16:11:31 2008
Categories: Eukaryota | Single protein | Hurley, J H. | Majerus, P W. | Miller, G J. | Wilson, M P. | ACP | I3S | MG | Atp-grasp | Inositol phosphate kinase
